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DCTN2_MOUSE
ID   DCTN2_MOUSE             Reviewed;         402 AA.
AC   Q99KJ8;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Dynactin subunit 2;
DE   AltName: Full=50 kDa dynein-associated polypeptide;
DE   AltName: Full=Dynactin complex 50 kDa subunit;
DE            Short=DCTN-50;
DE   AltName: Full=Growth cone membrane protein 23-48K;
DE            Short=GMP23-48K;
DE   AltName: Full=p50 dynamitin;
GN   Name=Dctn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 66-75; 78-92; 103-117; 157-171; 195-217 AND 310-321,
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   PubMed=9144527; DOI=10.1006/bbrc.1997.6447;
RA   Abe T.K., Tanaka H., Iwanaga T., Odani S., Kuwano R.;
RT   "The presence of the 50-kDa subunit of dynactin complex in the nerve growth
RT   cone.";
RL   Biochem. Biophys. Res. Commun. 233:295-299(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 320-333.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   INTERACTION WITH BICD2.
RX   PubMed=11483508; DOI=10.1093/emboj/20.15.4041;
RA   Hoogenraad C.C., Akhmanova A., Howell S.A., Dortland B.R., de Zeeuw C.I.,
RA   Willemsen R., Visser P., Grosveld F., Galjart N.;
RT   "Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-dynactin
RT   pathway by interacting with these complexes.";
RL   EMBO J. 20:4041-4054(2001).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP135.
RX   PubMed=14983524; DOI=10.1002/cm.10175;
RA   Uetake Y., Terada Y., Matuliene J., Kuriyama R.;
RT   "Interaction of Cep135 with a p50 dynactin subunit in mammalian
RT   centrosomes.";
RL   Cell Motil. Cytoskeleton 58:53-66(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-86, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-321, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   INTERACTION WITH BICD2.
RX   PubMed=22956769; DOI=10.1091/mbc.e12-03-0210;
RA   Splinter D., Razafsky D.S., Schlager M.A., Serra-Marques A., Grigoriev I.,
RA   Demmers J., Keijzer N., Jiang K., Poser I., Hyman A.A., Hoogenraad C.C.,
RA   King S.J., Akhmanova A.;
RT   "BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to
RT   cellular structures.";
RL   Mol. Biol. Cell 23:4226-4241(2012).
CC   -!- FUNCTION: Modulates cytoplasmic dynein binding to an organelle, and
CC       plays a role in prometaphase chromosome alignment and spindle
CC       organization during mitosis. Involved in anchoring microtubules to
CC       centrosomes. May play a role in synapse formation during brain
CC       development. {ECO:0000269|PubMed:14983524}.
CC   -!- SUBUNIT: Subunit of dynactin, a multiprotein complex associated with
CC       dynein. Interacts with ECPAS, DYNAP and MAPRE1 (By similarity).
CC       Interacts with BICD2 (PubMed:11483508, PubMed:22956769). Interacts with
CC       CEP135 (PubMed:14983524). {ECO:0000250|UniProtKB:Q13561,
CC       ECO:0000269|PubMed:11483508, ECO:0000269|PubMed:14983524,
CC       ECO:0000269|PubMed:22956769}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:14983524,
CC       ECO:0000269|PubMed:9144527}. Membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Present at high levels in both cytoplasmic and
CC       membrane-associated forms in neonates. Levels of membrane-associated
CC       form are greatly reduced in the adult. {ECO:0000269|PubMed:9144527}.
CC   -!- SIMILARITY: Belongs to the dynactin subunit 2 family. {ECO:0000305}.
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DR   EMBL; BC004613; AAH04613.1; -; mRNA.
DR   CCDS; CCDS24234.1; -.
DR   RefSeq; NP_081427.1; NM_027151.2.
DR   AlphaFoldDB; Q99KJ8; -.
DR   BioGRID; 213590; 51.
DR   CORUM; Q99KJ8; -.
DR   IntAct; Q99KJ8; 29.
DR   MINT; Q99KJ8; -.
DR   STRING; 10090.ENSMUSP00000026479; -.
DR   iPTMnet; Q99KJ8; -.
DR   PhosphoSitePlus; Q99KJ8; -.
DR   REPRODUCTION-2DPAGE; Q99KJ8; -.
DR   UCD-2DPAGE; Q99KJ8; -.
DR   EPD; Q99KJ8; -.
DR   jPOST; Q99KJ8; -.
DR   MaxQB; Q99KJ8; -.
DR   PaxDb; Q99KJ8; -.
DR   PRIDE; Q99KJ8; -.
DR   ProteomicsDB; 279604; -.
DR   Antibodypedia; 28711; 385 antibodies from 35 providers.
DR   DNASU; 69654; -.
DR   Ensembl; ENSMUST00000026479; ENSMUSP00000026479; ENSMUSG00000025410.
DR   GeneID; 69654; -.
DR   KEGG; mmu:69654; -.
DR   UCSC; uc007hiu.2; mouse.
DR   CTD; 10540; -.
DR   MGI; MGI:107733; Dctn2.
DR   VEuPathDB; HostDB:ENSMUSG00000025410; -.
DR   eggNOG; KOG3958; Eukaryota.
DR   GeneTree; ENSGT00390000003427; -.
DR   HOGENOM; CLU_049964_1_0_1; -.
DR   InParanoid; Q99KJ8; -.
DR   OMA; RGYDMRG; -.
DR   OrthoDB; 951183at2759; -.
DR   PhylomeDB; Q99KJ8; -.
DR   TreeFam; TF105247; -.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR   BioGRID-ORCS; 69654; 29 hits in 74 CRISPR screens.
DR   ChiTaRS; Dctn2; mouse.
DR   PRO; PR:Q99KJ8; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q99KJ8; protein.
DR   Bgee; ENSMUSG00000025410; Expressed in spermatocyte and 260 other tissues.
DR   ExpressionAtlas; Q99KJ8; baseline and differential.
DR   Genevisible; Q99KJ8; MM.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005869; C:dynactin complex; ISO:MGI.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0000776; C:kinetochore; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR   GO; GO:0032402; P:melanosome transport; IMP:MGI.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
DR   GO; GO:0007080; P:mitotic metaphase plate congression; ISO:MGI.
DR   GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR   GO; GO:0071539; P:protein localization to centrosome; ISO:MGI.
DR   InterPro; IPR028133; Dynamitin.
DR   PANTHER; PTHR15346; PTHR15346; 1.
DR   Pfam; PF04912; Dynamitin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Dynein; Membrane; Microtubule; Phosphoprotein;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q13561"
FT   CHAIN           2..402
FT                   /note="Dynactin subunit 2"
FT                   /id="PRO_0000079822"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          99..132
FT                   /evidence="ECO:0000255"
FT   COILED          215..245
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13561"
FT   MOD_RES         6
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13561"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         86
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   MOD_RES         134
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13561"
FT   MOD_RES         321
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   402 AA;  44117 MW;  EA0D8E04E92726AC CRC64;
     MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELSS TSVEHIIVNP NAAYDKFKDK
     RVGTKGLDFS DRIGKTKRTG YESGDYEMLG EGLGVKETPQ QKYQRLLHEV QELTTEVEKI
     KTTVKESATE EKLTPVVLAK QLAALKQQLV ASHLEKLLGP DAAINLADPD GALAKRLLLQ
     LEATKSSKGS SGGKATAGAP PDSSLVTYEL HSRPEQDKFS QAAKVAELEK RLTELEATVR
     CDQDAQNPLS AGLQGACLME TVELLQAKVS ALDLAVLDQV EARLQSVLGK VNEIAKHKAS
     VEDADTQNKV HQLYETIQRW SPVASTLPEL VQRLVTIKQL HEQAMQFGQL LTHLDTTQQM
     MASSLKDNTA LLTQVQTTMR ENLATVEGNF ASIDARMKRL GK
 
 
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